1.2.1.19: aminobutyraldehyde dehydrogenase
This is an abbreviated version!
For detailed information about aminobutyraldehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.19
-
1.2.1.19
-
badhs
-
choline
-
osmoprotectant
-
1.2.1.8
-
spinacia
-
2-acetyl-1-pyrroline
-
glycinebetaine
-
3-aminopropionaldehyde
-
suaeda
-
halophyte
-
fragrant
-
hypochondriacus
-
aldh10s
-
amaranthus
-
liaotungensis
-
jasmine
-
basmati
-
4-aminobutyrate
-
synthesis
- 1.2.1.19
-
badhs
- choline
-
osmoprotectant
-
1.2.1.8
-
spinacia
-
2-acetyl-1-pyrroline
- glycinebetaine
- 3-aminopropionaldehyde
-
suaeda
-
halophyte
-
fragrant
-
hypochondriacus
- aldh10s
-
amaranthus
-
liaotungensis
-
jasmine
-
basmati
- 4-aminobutyrate
- synthesis
Reaction
Synonyms
4-aminobutanal dehydrogenase, 4-aminobutyraldehyde dehydrogenase, ABAL dehydrogenase, ABALDH, ALDH10A8, ALDH10A9, AMADH, AMADH1, AMADH2, aminoaldehyde dehydrogenase, BADH, betaine aldehyde dehydrogenase, dehydrogenase, aminobutyraldehyde, EC 1.5.1.35, gadbh, gamma-aminobutanal dehydrogenase, gamma-aminobutyraldehyde dehydroganase, gamma-aminobutyraldehyde dehydrogenase, gamma-guanidinobutyraldehyde dehydrogenase, MdAMADH1, MdAMADH2, More, NAD+-aminoaldehyde dehydrogenase, NAD+-dependent aminoaldehyde dehydrogenase, PatD, PsAMADH 1, PsAMADH 2, SlAMADH1, SlAMADH2, YdcW, ZmAMADH1a, ZmAMADH1b, ZmAMADH2
ECTree
Advanced search results
Subunits
Subunits on EC 1.2.1.19 - aminobutyraldehyde dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
dimer
tetramer
dimer
plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site
dimer
plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site